DAP10 Protein, Human (HEK293, mFc)

DAP10, a transmembrane adapter protein, forms an activation receptor, KLRK1-HCST, in lymphoid and myeloid cells, playing a pivotal role in triggering cytotoxicity against target cells expressing stress-induced ligands such as MHC class I chain-related MICA and MICB, as well as UL16-binding proteins (ULBPs). This receptor, activated by the interaction of ULBPs with KLRK1-HCST, initiates calcium mobilization and activates the PI3-kinase PIK3R1, MAP2K/ERK, and JAK2/STAT5 signaling pathways. The presence of both PIK3R1 and GRB2 is essential for full KLRK1-HCST-mediated activation, leading to the ultimate killing of target cells. In NK cells, KLRK1-HCST signaling induces cytotoxicity and enhances cytokine production, while in T-cells, it primarily provides costimulation for TCR-induced signals. The KLRK1-HCST receptor plays a crucial role in immune surveillance against tumors, and its absence results in the escape of melanoma cells from NK cell-mediated immune surveillance. DAP10 interacts with CLEC5A, forming a CLEC5A/TYROBP/HCST trimolecular complex, and it homodimerizes, with disulfide linkages. The heterohexamer comprises four subunits of HCST/DAP10 and two subunits of KLRK1, and it interacts with PIK3R1, GRB2, KLRK1, and CD300H.